4CBW: Actin, alpha skeletal muscle, actin

Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin. Determined by X-ray diffraction at 2.5 Å resolution. Released 30 Apr 2014.

Method
X-ray diffraction
Resolution
2.5 Å
Organisms
PLASMODIUM BERGHEI, SYNTHETIC CONSTRUCT, MUS MUSCULUS
Chains
2
Atoms
3,956
Mol. weight
56.87 kDa
Ligands
CA, DIO, ATP
Released
30 Apr 2014

Explore 4CBW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CBW contains 33 α-helices and 28 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 27 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix7-82
β-strand9-1241
β-strand17-2261
β-strand30-3341
β-strand36-3942
β-strand54-5522
α-helix57-604
α-helix63-653
β-strand66-6942
β-strand72-7323
β-strand76-7723
α-helix80-889
α-helix89-957
α-helix99-1013
β-strand104-10851
α-helix114-12613
β-strand132-13761
α-helix138-1458
β-strand151-15664
β-strand161-16774
β-strand170-17124
α-helix173-1753
β-strand177-17934
α-helix183-19311
α-helix194-1974
α-helix206-21712
β-strand21915
α-helix224-23310
β-strand239-24246
β-strand248-25146
α-helix254-2574
α-helix259-2624
α-helix265-2684
α-helix272-2743
α-helix275-28410
α-helix288-2903
α-helix291-2955
β-strand298-30144
α-helix303-3064
β-strand30815
α-helix310-32112
β-strand330-33124
α-helix339-3479
α-helix353-3553
β-strand358-35921
α-helix360-3667
α-helix368-3703
α-helix371-3744
Chain G: 6 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix30-345
β-strand40-4677
β-strand51-5337
α-helix54-552
α-helix56-583
β-strand61-6338
β-strand67-7597
β-strand81-8997
α-helix95-11117
β-strand116-12277
α-helix128-1314
β-strand139-14138
α-helix145-1473

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscle, actinAprotein377PLASMODIUM BERGHEI, SYNTHETIC CONSTRUCTP68137 (AlphaFold model), Q4Z1L3 (AlphaFold model)
GelsolinGprotein127MUS MUSCULUSP13020 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4CBW_1 ACTIN, ALPHA SKELETAL MUSCLE, ACTIN (chains A)
GAGDEEVQALVIDNGSGNVKAGVAGDDAPRSVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRER
MTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRL
DLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEK
SYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIV
LSGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWIT
KEEYDESGPSIVHRKCF
Sequence of entity 2 (G), FASTA
>4CBW_2 GELSOLIN (chains G)
GPMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQ
YDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFSGYFKSGLKYKK
GGVASGF

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa3
DIO1,4-diethylene dioxideC4 H8 O21
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31

Primary citation

Structural Differences Explain Diverse Functions of Plasmodium Actins. Vahokoski, J., Bhargav, S.P., Desfosses, A. et al. PLoS Pathog (2014) 10:4091. DOI 10.1371/JOURNAL.PPAT.1004091 · PubMed

Other PDB entries of the same protein (UniProt P68137 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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